2H8A

Structure of Microsomal Glutathione Transferase 1 in Complex with Glutathione

Summary for 2H8A

• Entry DOI: 10.2210/pdb2h8a/pdb
• Descriptor: Microsomal glutathione S-transferase 1, GLUTATHIONE (2 entities in total)
• Functional Keywords: membrane protein, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Microsome: P08011
• Total number of polymer chains: 1
• Total formula weight: 17668.61

Authors

Hebert, H. (deposition date: 2006-06-07, release date: 2007-05-22, Last modification date: 2024-02-14)

Primary citation

Holm, P.J.,Bhakat, P.,Jegerschold, C.,Gyobu, N.,Mitsuoka, K.,Fujiyoshi, Y.,Morgenstern, R.,Hebert, H.
Structural basis for detoxification and oxidative stress protection in membranes.
J.Mol.Biol., 360:934-945, 2006

PubMed Abstract: Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat microsomal glutathione transferase 1, at 3.2 A resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.

PubMed: 16806268
DOI: 10.1016/j.jmb.2006.05.056

Experimental method

ELECTRON CRYSTALLOGRAPHY (3.2 Å)